Purification and biochemical characterization of two detergent-stable serine alkaline proteases from Streptomyces sp. strain AH4

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• 作者：Souraya Boulkour Touioui…
• 关键词：Proteases ; Streptomyces ; Purification ; MALDI ; TOF/MS ; Laundry detergent
• 刊名：World Journal of Microbiology & Biotechnology
• 出版年：2015
• 出版时间：July 2015
• 年：2015
• 卷：31
• 期：7
• 页码：1079-1092
• 全文大小：1,001 KB
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• 作者单位：Souraya Boulkour Touioui (1) (2)
  Nadia Zara? Jaouadi (3)
  Hadjira Boudjella (1)
  Fatma Zohra Ferradji (4)
  Mouna Belhoul (3)
  Hatem Rekik (3)
  Abdelmalek Badis (4) (5)
  Samir Bejar (2)
  Bassem Jaouadi (2)
  
  1. Laboratory of Microbial Systems Biology (LMSB), école Normale Supérieure (ENS) de Kouba, PO Box 92, 16050, Kouba, Algiers, Algeria
  2. Laboratory of Natural Products Chemistry and Biomolecules (LNPCB), University of Blida, 1, Road of Soumaa, PO Box 270, 09000, Blida, Algeria
  3. Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, PO Box 1177, 3018, Sfax, Tunisia
  4. National Centre for Research and Development of Fisheries and Aquaculture (CNRDPA), 11, Bd Amirouche, PO Box 67, 42415, Bou Isma?l, Tipaza, Algeria
  5. Laboratory of Natural Substances Chemistry and Biomolecules, University of Blida, 1, Road of Soumaa, PO Box 270, 09000, Blida, Algeria
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Applied Microbiology
  Biotechnology
  Biochemistry
  Environmental Biotechnology
  Microbiology
  
• 出版者：Springer Netherlands
• ISSN：1573-0972

文摘

Streptomyces sp. strain AH4 exhibited a high ability to produce two extracellular proteases when cultured on a yeast malt-extract (ISP2)-casein-based medium. Pure proteins were obtained after heat treatment (30?min at 70?°C) and ammonium sulphate fractionation (30-0?%), followed by size exclusion HPLC column. Matrix assisted laser desorption ionization-time of flight mass spectrometry analysis revealed that the purified enzymes (named SAPS-P1 and SAPS-P2) were monomers with molecular masses of 36,417.13 and 21,099.10?Da, respectively. Their identified N-terminal amino acid displayed high homologies with those of Streptomyces proteases. While SAPS-P1 was optimally active at pH 12.0 and 70?°C, SAPS-P2 showed optimum activity at pH 10.0 and 60?°C. Both enzymes were completely stable within a wide range of temperature (45-5?°C) and pH (8.0-1.5). They were noted to be completely inhibited by phenylmethanesulfonyl fluoride and diisopropyl fluorophosphates, which confirmed their belonging to the serine proteases family. Compared to SAPS-P2, SAPS-P1 showed high thermostability and excellent stability towards bleaching, denaturing, and oxidizing agents. Both enzymes displayed marked stability and compatibility with a wide range of commercial laundry detergents and significant catalytic efficiencies compared to Subtilisin Carlsberg and Protease SG-XIV. Overall, the results indicated that SAPS-P1 and SAPS-P2 can be considered as potential promising candidates for future application as bioadditives in detergent formulations.